Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Respiratory nitrate reductase 1 beta chain

Gene

narH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit.

Catalytic activityi

Nitrate + a quinol = nitrite + a quinone + H2O.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi16Iron-sulfur 1 (4Fe-4S)2 Publications1
Metal bindingi19Iron-sulfur 1 (4Fe-4S)2 Publications1
Metal bindingi22Iron-sulfur 1 (4Fe-4S)2 Publications1
Metal bindingi26Iron-sulfur 2 (4Fe-4S)2 Publications1
Metal bindingi184Iron-sulfur 3 (4Fe-4S)2 Publications1
Metal bindingi187Iron-sulfur 3 (4Fe-4S)2 Publications1
Metal bindingi192Iron-sulfur 3 (4Fe-4S)2 Publications1
Metal bindingi196Iron-sulfur 4 (3Fe-4S)2 Publications1
Metal bindingi217Iron-sulfur 4 (3Fe-4S)2 Publications1
Metal bindingi223Iron-sulfur 4 (3Fe-4S)2 Publications1
Metal bindingi227Iron-sulfur 3 (4Fe-4S)2 Publications1
Metal bindingi244Iron-sulfur 2 (4Fe-4S)2 Publications1
Metal bindingi247Iron-sulfur 2 (4Fe-4S)2 Publications1
Metal bindingi259Iron-sulfur 2 (4Fe-4S)2 Publications1
Metal bindingi263Iron-sulfur 1 (4Fe-4S)2 Publications1

GO - Molecular functioni

  • 3 iron, 4 sulfur cluster binding Source: EcoCyc
  • 4 iron, 4 sulfur cluster binding Source: EcoCyc
  • electron transfer activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW
  • nitrate reductase activity Source: EcoCyc

GO - Biological processi

  • anaerobic respiration Source: EcoCyc
  • nitrate assimilation Source: UniProtKB-KW
  • nitrate metabolic process Source: EcoCyc

Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Nitrate assimilation, Transport
Ligand3Fe-4S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:NARH-MONOMER
MetaCyc:NARH-MONOMER
BRENDAi1.7.5.1 2026

Protein family/group databases

TCDBi5.A.3.1.1 the prokaryotic molybdopterin-containing oxidoreductase (pmo) family

Names & Taxonomyi

Protein namesi
Recommended name:
Respiratory nitrate reductase 1 beta chain (EC:1.7.5.1)
Alternative name(s):
Nitrate reductase A subunit beta
Quinol-nitrate oxidoreductase subunit beta
Gene namesi
Name:narH
Ordered Locus Names:b1225, JW1216
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10639 narH

Subcellular locationi

GO - Cellular componenti

  • intrinsic component of membrane Source: EcoCyc
  • intrinsic component of the cytoplasmic side of the plasma membrane Source: EcoCyc
  • membrane Source: UniProtKB
  • NarGHI complex Source: EcoCyc

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry databases

DrugBankiDB04464 N-Formylmethionine

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000967201 – 512Respiratory nitrate reductase 1 beta chainAdd BLAST512

Proteomic databases

PaxDbiP11349
PRIDEiP11349

Expressioni

Inductioni

By nitrate.

Interactioni

Subunit structurei

Dimer of heterotrimers each composed of an alpha, a beta and a gamma chain. Alpha and beta are catalytic chains; gamma chains are involved in binding the enzyme complex to the cytoplasmic membrane.1 Publication

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi4262231, 28 interactors
ComplexPortaliCPX-1974 Nitrate reductase A
DIPiDIP-10312N
IntActiP11349, 15 interactors
STRINGi316385.ECDH10B_1284

Structurei

Secondary structure

1512
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 12Combined sources10
Turni13 – 15Combined sources3
Helixi21 – 30Combined sources10
Beta strandi41 – 49Combined sources9
Turni51 – 57Combined sources7
Helixi59 – 62Combined sources4
Beta strandi65 – 68Combined sources4
Beta strandi74 – 76Combined sources3
Helixi81 – 85Combined sources5
Turni86 – 89Combined sources4
Helixi97 – 100Combined sources4
Beta strandi104 – 106Combined sources3
Helixi109 – 113Combined sources5
Beta strandi126 – 128Combined sources3
Turni129 – 131Combined sources3
Turni142 – 148Combined sources7
Helixi152 – 155Combined sources4
Helixi159 – 161Combined sources3
Helixi167 – 170Combined sources4
Helixi172 – 174Combined sources3
Beta strandi178 – 182Combined sources5
Helixi191 – 194Combined sources4
Beta strandi201 – 204Combined sources4
Turni205 – 207Combined sources3
Beta strandi210 – 212Combined sources3
Turni214 – 216Combined sources3
Helixi223 – 226Combined sources4
Beta strandi232 – 235Combined sources4
Turni236 – 239Combined sources4
Beta strandi240 – 243Combined sources4
Helixi248 – 251Combined sources4
Turni252 – 254Combined sources3
Helixi258 – 261Combined sources4
Beta strandi268 – 276Combined sources9
Helixi277 – 279Combined sources3
Helixi280 – 284Combined sources5
Helixi289 – 291Combined sources3
Helixi292 – 297Combined sources6
Helixi306 – 314Combined sources9
Helixi319 – 325Combined sources7
Helixi329 – 334Combined sources6
Beta strandi341 – 343Combined sources3
Helixi345 – 347Combined sources3
Beta strandi352 – 356Combined sources5
Beta strandi366 – 368Combined sources3
Helixi380 – 382Combined sources3
Beta strandi383 – 385Combined sources3
Helixi387 – 394Combined sources8
Helixi399 – 420Combined sources22
Helixi428 – 432Combined sources5
Helixi437 – 447Combined sources11
Helixi452 – 455Combined sources4
Turni463 – 466Combined sources4
Helixi469 – 475Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q16X-ray1.90B1-512[»]
1R27X-ray2.00B/D1-512[»]
1SIWX-ray2.20B1-512[»]
1Y4ZX-ray2.00B1-512[»]
1Y5IX-ray1.90B1-512[»]
1Y5LX-ray2.50B1-512[»]
1Y5NX-ray2.50B1-512[»]
3EGWX-ray1.90B1-509[»]
3IR5X-ray2.30B1-512[»]
3IR6X-ray2.80B1-512[»]
3IR7X-ray2.50B1-512[»]
ProteinModelPortaliP11349
SMRiP11349
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11349

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 354Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd BLAST29
Domaini175 – 2064Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd BLAST32
Domaini208 – 2374Fe-4S ferredoxin-type 3PROSITE-ProRule annotationAdd BLAST30

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4108IUE Bacteria
COG1140 LUCA
HOGENOMiHOG000237353
InParanoidiP11349
KOiK00371
OMAiVYFNWQT
PhylomeDBiP11349

Family and domain databases

CDDicd10557 NarH_beta-like, 1 hit
Gene3Di1.10.3650.10, 1 hit
InterProiView protein in InterPro
IPR017896 4Fe4S_Fe-S-bd
IPR029263 Nitr_red_bet_C
IPR038262 Nitr_red_bet_C_sf
IPR006547 NO3_Rdtase_bsu
PfamiView protein in Pfam
PF13247 Fer4_11, 1 hit
PF14711 Nitr_red_bet_C, 1 hit
TIGRFAMsiTIGR01660 narH, 1 hit
PROSITEiView protein in PROSITE
PS51379 4FE4S_FER_2, 3 hits

Sequencei

Sequence statusi: Complete.

P11349-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIRSQVGMV LNLDKCIGCH TCSVTCKNVW TSREGVEYAW FNNVETKPGQ
60 70 80 90 100
GFPTDWENQE KYKGGWIRKI NGKLQPRMGN RAMLLGKIFA NPHLPGIDDY
110 120 130 140 150
YEPFDFDYQN LHTAPEGSKS QPIARPRSLI TGERMAKIEK GPNWEDDLGG
160 170 180 190 200
EFDKLAKDKN FDNIQKAMYS QFENTFMMYL PRLCEHCLNP ACVATCPSGA
210 220 230 240 250
IYKREEDGIV LIDQDKCRGW RMCITGCPYK KIYFNWKSGK SEKCIFCYPR
260 270 280 290 300
IEAGQPTVCS ETCVGRIRYL GVLLYDADAI ERAASTENEK DLYQRQLDVF
310 320 330 340 350
LDPNDPKVIE QAIKDGIPLS VIEAAQQSPV YKMAMEWKLA LPLHPEYRTL
360 370 380 390 400
PMVWYVPPLS PIQSAADAGE LGSNGILPDV ESLRIPVQYL ANLLTAGDTK
410 420 430 440 450
PVLRALKRML AMRHYKRAET VDGKVDTRAL EEVGLTEAQA QEMYRYLAIA
460 470 480 490 500
NYEDRFVVPS SHRELAREAF PEKNGCGFTF GDGCHGSDTK FNLFNSRRID
510
AIDVTSKTEP HP
Length:512
Mass (Da):58,066
Last modified:February 1, 1996 - v3
Checksum:i2E7719C8D078BAEA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti398 – 417DTKPV…RHYKR → EYQTGTARTETYAGDASLQT in AAA24195 (PubMed:2832376).CuratedAdd BLAST20

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20147 Genomic DNA Translation: AAA24195.1
U00096 Genomic DNA Translation: AAC74309.1
AP009048 Genomic DNA Translation: BAA36095.1
X16181 Genomic DNA Translation: CAA34304.1
PIRiF64869 RDECNB
RefSeqiNP_415743.1, NC_000913.3
WP_000702650.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC74309; AAC74309; b1225
BAA36095; BAA36095; BAA36095
GeneIDi945780
KEGGiecj:JW1216
eco:b1225
PATRICifig|1411691.4.peg.1056

Similar proteinsi

Entry informationi

Entry nameiNARH_ECOLI
AccessioniPrimary (citable) accession number: P11349
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 1, 1996
Last modified: June 20, 2018
This is version 176 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health